ID A0A1Y3YC41_9FIRM Unreviewed; 487 AA.
AC A0A1Y3YC41;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Alpha-glucosidase/alpha-galactosidase {ECO:0000313|EMBL:OUN93017.1};
GN ORFNames=B5G00_07635 {ECO:0000313|EMBL:OUN93017.1};
OS Blautia sp. An46.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX NCBI_TaxID=1965636 {ECO:0000313|EMBL:OUN93017.1, ECO:0000313|Proteomes:UP000196301};
RN [1] {ECO:0000313|Proteomes:UP000196301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An46 {ECO:0000313|Proteomes:UP000196301};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000256|RuleBase:RU361152};
CC Note=Binds 1 NAD(+) per subunit. {ECO:0000256|RuleBase:RU361152};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 4 family.
CC {ECO:0000256|ARBA:ARBA00010141, ECO:0000256|RuleBase:RU361152}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OUN93017.1}.
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DR EMBL; NFIF01000007; OUN93017.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y3YC41; -.
DR OrthoDB; 9808275at2; -.
DR Proteomes; UP000196301; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd05297; GH4_alpha_glucosidase_galactosidase; 1.
DR Gene3D; 3.90.1820.10; AglA-like glucosidase; 1.
DR InterPro; IPR019802; GlycHydrolase_4_CS.
DR InterPro; IPR001088; Glyco_hydro_4.
DR InterPro; IPR022616; Glyco_hydro_4_C.
DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR32092; 6-PHOSPHO-BETA-GLUCOSIDASE-RELATED; 1.
DR PANTHER; PTHR32092:SF6; ALPHA-GALACTOSIDASE; 1.
DR Pfam; PF02056; Glyco_hydro_4; 1.
DR Pfam; PF11975; Glyco_hydro_4C; 1.
DR PRINTS; PR00732; GLHYDRLASE4.
DR SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS01324; GLYCOSYL_HYDROL_F4; 1.
PE 3: Inferred from homology;
KW Cobalt {ECO:0000256|PIRSR:PIRSR601088-3};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361152};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361152};
KW Iron {ECO:0000256|PIRSR:PIRSR601088-3};
KW Manganese {ECO:0000256|PIRSR:PIRSR601088-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR601088-3};
KW NAD {ECO:0000256|RuleBase:RU361152};
KW Nickel {ECO:0000256|PIRSR:PIRSR601088-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000196301}.
FT DOMAIN 195..413
FT /note="Glycosyl hydrolase family 4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11975"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 170
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT BINDING 200
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT SITE 110
FT /note="Increases basicity of active site Tyr"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ SEQUENCE 487 AA; 55146 MW; 164224D490551A8B CRC64;
MSFKVAFIGA GSLVFARTLF TDIMSVPEFH NIEVAFTDIN EDNLEKTRAL CQRDLDANGI
PVKIFATTDR REAFRDARYI VNCVRIGGLE AFETDIEIPL KYGVDQCVGD TLCTGGIMYG
QRVIAEMLNF CKDIREVAEP GAIMLNYSNP NAMATWACNK YGGVKTIGLC HGEIHGEMQI
AEVLGIPREE LDIICAGINH QTWYISVKHH GEDMIPKLLE GFENHEKFRE EEKVRIDMLK
RFGYYSTESN GHLSEYVAWY RKRPDEIKDW INLDNWINGE TGGYLRVTRE ERNWFETDYP
KILKEEPKKL DGSERGKEHC SYIIESLETG RMYRGHFNMM NEGCITNLPY ESVVEVPCYV
DGNGISVPKV GDLPLGCAAV CSQSIWVQKL AVEAAVHGDV KLLKQAAMMD PLTGAVCNPP
EIWQMIDEML VAQEKWLPQY TEAIKEAKEN LAKGDLIPTK DYHGAARLRE KTPEEVAAEH
EARKITV
//
